GenomeNet

Database: UniProt
Entry: T1HU97_RHOPR
LinkDB: T1HU97_RHOPR
Original site: T1HU97_RHOPR 
ID   T1HU97_RHOPR            Unreviewed;       447 AA.
AC   T1HU97;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 2.
DT   24-JAN-2024, entry version 50.
DE   RecName: Full=glutaminase {ECO:0000256|ARBA:ARBA00012918};
DE            EC=3.5.1.2 {ECO:0000256|ARBA:ARBA00012918};
DE   Flags: Fragment;
OS   Rhodnius prolixus (Triatomid bug).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Paraneoptera; Hemiptera; Heteroptera; Panheteroptera;
OC   Cimicomorpha; Reduviidae; Triatominae; Rhodnius.
OX   NCBI_TaxID=13249 {ECO:0000313|EnsemblMetazoa:RPRC007617-PA, ECO:0000313|Proteomes:UP000015103};
RN   [1] {ECO:0000313|Proteomes:UP000015103}
RP   NUCLEOTIDE SEQUENCE.
RA   Wilson R.K., Warren W., Dotson E., Oliveira P.L.;
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:RPRC007617-PA}
RP   IDENTIFICATION.
RG   EnsemblMetazoa;
RL   Submitted (MAY-2015) to UniProtKB.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC         Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001062};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC   -!- SIMILARITY: Belongs to the glutaminase family.
CC       {ECO:0000256|ARBA:ARBA00011076}.
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DR   EMBL; ACPB03000737; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; T1HU97; -.
DR   STRING; 13249.T1HU97; -.
DR   EnsemblMetazoa; RPRC007617-RA; RPRC007617-PA; RPRC007617.
DR   VEuPathDB; VectorBase:RPRC007617; -.
DR   eggNOG; KOG0506; Eukaryota.
DR   HOGENOM; CLU_654854_0_0_1; -.
DR   InParanoid; T1HU97; -.
DR   OrthoDB; 3151390at2759; -.
DR   Proteomes; UP000015103; Unassembled WGS sequence.
DR   GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:InterPro.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR015868; Glutaminase.
DR   PANTHER; PTHR12544; GLUTAMINASE; 1.
DR   PANTHER; PTHR12544:SF29; GLUTAMINASE; 1.
DR   Pfam; PF04960; Glutaminase; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 1.
PE   3: Inferred from homology;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000015103}.
FT   REPEAT          372..404
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
SQ   SEQUENCE   447 AA;  50102 MW;  72A69AD9F4B91AFC CRC64;
     MVIPKFEELR HAVGVLYGEI EGDVTGETSN YIPEIKNTCP DLWAVSICST DGQKCSFGDY
     LVPLTIQDIS YPFLYAKCLD LFGSATVLEY VGIERKPADV SVKNSKANNR AFNPMTDSGA
     ISLSTLFCDN DKRTGTAADK HYEFFEFMKA LCGNNHFQIC TPAYVSVRQK DDLSRSIAYA
     MLNQGHLPND TDIPTIMDFY FEARSLEVTC DGLAVMAATL ANFGVNPYTN EKLISPISVK
     AVLSAMHNWG NYGYSGVNAF YLGLPSKHSV AGAFMVVVPG MLGLILYSPR INDNEVGEKN
     IDFAMKFVKK FDLHPLSNSS KEMKKRFGTR KIPEVPCENY CKIFTAVFNN DLEEVMNLTK
     GNKKIVFEKD LEGRTILHLA AIKGHFEIIK FVTSNFRKLS SVKDRFGRVP REYVKASDKN
     FFEITNIFKK WEDLDKICEL ASASNIN
//
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